Enhancement of pea protein solubility and thermal stability for acidic beverage applications via endogenous Maillard-induced glycation and chromatography purification

Development of low‐fat Mozzarella cheeses enriched with soy or pea protein hydrolysates: Composition, texture and functional properties during ageing

“…That is, the protein content of whey was 0.98%, which increased to 3.92% on raising the concentration of SPH from 0 to 8% and increased to 3.86% on raising the concentration of PPH to 8%. Soy proteins and pea proteins have low solubility, especially in milk at near-neutral pH, showing weak potential to be used in cheese milk (O Flynn et al 2021;Schneider et al 2023). However, our study demonstrated that SPH and PPH can be added to cheese milk at a proportion of 8% and then the resulting solution can be made into LFC, suggesting that SPH and PPH are superior plant-based ingredients to replace milk protein compared with soy and pea proteins.…”

“…2021; Schneider et al . 2023). However, our study demonstrated that SPH and PPH can be added to cheese milk at a proportion of 8% and then the resulting solution can be made into LFC, suggesting that SPH and PPH are superior plant‐based ingredients to replace milk protein compared with soy and pea proteins.…”

Molecular forces driving protein complexation of lentil and whey proteins: Structure-function relationships of trehalose-conjugated protein complexes on protein digestibility and solubility

“…This water displacement can help protect the protein structure by reducing water-mediated interactions that may lead to denaturation ( Wang et al, 2023 ). Glycosylation adds bulky carbohydrate groups to the protein molecule ( Schneider et al, 2023 ). These bulky groups can provide steric hindrance, preventing or inhibiting the unfolding of the protein structure ( Ke & Li, 2023 ; Higa & Nickerson, 2023 ).…”

Effects of Heat Treatment on the Structural and Functional Properties of Phaseolus vulgaris L. Protein

“…A moderate heating treatment may enhance the ability of PVP to combine with water because it opens the structure and exposes the hydrophilic groups [58]. If the heat treatment time is too long, the thermal aggregation between PVP molecules increases the intermolecular force, reducing PVP's ability to combine with water, thus reducing its solubility [59]. Bogahawaththa et al [60] reported that specific heating temperature and time combinations can have distinct effects on protein solubility.…”